Hydrolysis of the phosphoanhydride linkage of cyclic ADP‐ribose by the Mn2+‐dependent ADP‐ribose/CDP‐alcohol pyrophosphatase

• Published in: FEBS letters Vol. 583; no. 10; pp. 1593 - 1598
• Main Authors: Canales, José, Fernández, Ascensión, Rodrigues, Joaquim Rui, Ferreira, Rui, Ribeiro, João Meireles, Cabezas, Alicia, Costas, María Jesús, Cameselle, José Carlos
• Format: Journal Article
• Language: English
• Published: 19.05.2009
• Subjects: ADP-ribose; ADPRibase-Mn; cADPR; cyclic ADP-ribose; dimethylsulfoxide; DMSO; Histidine biosynthesis; Immune signaling; Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase; N 1-(5-phosphoribosyl)-adenosine; N 1-(5-phosphoribosyl)-adenosine 5′-monophosphate; N 1-(5-phosphoribosyl)-adenosine 5′-triphosphate; N 1-(ribosyl)-adenosine; N 1-(ribosyl)-adenosine 5′-monophosphate; NAD glycohydrolase; NADase; Phosphoribosyl-AMP; pRib-Ado; pRib-AMP; pRib-ATP; Pyrophosphatase; Rib-Ado; Rib-AMP

Cyclic ADP‐ribose (cADPR) metabolism in mammals is catalyzed by NAD glycohydrolases (NADases) that, besides forming ADP‐ribose, form and hydrolyze the N 1‐glycosidic linkage of cADPR. Thus far, no cADPR phosphohydrolase was known. We tested rat ADP‐ribose/CDP‐alcohol pyrophosphatase (ADPRibase‐Mn) a...